Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 8.2, Problem 1BC
Summary Introduction
To analyze:
The similarity and difference between the ligand binding to receptor and enzyme binding to the substrate.
Introduction:
A signal transduction pathway includes a group of proteins and polysaccharides that carry the signals by the binding of the signaling molecule with the receptor. The signals carried, leads to conformational changes in the proteins, further trigger a cascade of reactions leading to a cellular response.
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Students have asked these similar questions
In the diagram below, the orange circle represents an effector and the dark purple shapes
(both the diamond and the rod) represent a substrate.
Based on this information, which statement(s) about the diagram is/are true? Select all
that apply.
A
Allosteric
site
B
Allosteric
site
C
Allosteric
site
Allosteric
effector
Active site
Allosteric
effector
Active site,
Allosteric
effector
Novel
binding
site
The Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the
dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins
would be more easily inhibited by an antagonist?
1.0
Y 0.5
2
A
4
6
B
8
[L] (μM)
10
12
14
16
Which of the following statements is/are correct?a) Enzyme quantities depend on the rate of their synthesis and degradationb) Enzyme quantity is decreased if an amino-acid involved in the catalytic activity is modifiedc) Protein kinase A activity is regulated through protein interaction.d) Kinases control the activity of other enzymes by covalent modification; irreversiblephosphorylation
explain each of the following option
Chapter 8 Solutions
Principles of Biology
Ch. 8.1 - What is the signaling molecule in this example?Ch. 8.1 - Prob. 2CCCh. 8.1 - Prob. 3CCCh. 8.1 - A general reason for cell signaling is to respond...Ch. 8.1 - Prob. 2TYKCh. 8.1 - Prob. 3TYKCh. 8.2 - Prob. 1BCCh. 8.2 - Prob. 1TYKCh. 8.2 - Prob. 2TYKCh. 8.3 - Prob. 1CC
Ch. 8.3 - What has to happen for the a and subunits of the...Ch. 8.3 - Prob. 1TYKCh. 8.3 - After a G-protein-coupled receptor is activated,...Ch. 8.4 - Prob. 1TYKCh. 8.5 - Look ahead to Figures 13.9 and, in particular,...Ch. 8.5 - Prob. 1TYKCh. 8.5 - Prob. 2TYKCh. 8.6 - Prob. 1CCCh. 8.6 - Prob. 2CCCh. 8.6 - Prob. 3CCCh. 8.6 - Prob. 1TYKCh. 8.6 - Prob. 2TYKCh. 8 - Prob. 1TYCh. 8 - Prob. 2TYCh. 8 - Prob. 3TYCh. 8 - Prob. 4TYCh. 8 - Which of the following is not an example of a cell...Ch. 8 - Prob. 6TYCh. 8 - The EGF receptor functions as a receptor tyrosine...Ch. 8 - Prob. 8TYCh. 8 - Prob. 9TYCh. 8 - The benefit of second messengers in signal...Ch. 8 - Prob. 1CCQCh. 8 - Prob. 2CCQCh. 8 - Prob. 3CCQCh. 8 - Discuss and compare several different types of...Ch. 8 - Prob. 2CBQ
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Which of the following is true as it relates to the phosphorylation of enzymes? a) Phosphorylation of an enzyme changes its activity. b) Phosphates can be added to R groups of any amino acid. c) Phosphate groups are added by a class of enzymes known as kinases. d) a and c e) a, b and carrow_forwardWhat is meant by a binding site? Select one: The area of a macromolecule target that is occupied by a chemical messenger when it binds The area of a macromolecule target that is occupied by a drug when it binds The area of a macromolecule target that is occupied by an agonist when it binds All the answers are correctarrow_forwardDraw the Lock and Key theory for protein active sites. Then draw what an inhibitor might look-like based on this modelarrow_forward
- 1. Allosteric regulation is an important part of feedback regulation. All of the functions listed below can be performed by an allosteric molecule EXCEPT: A) catalysis of a reaction. B) activation of an enzyme. C) inhibition of an enzyme. D) conformational change of an enzyme.arrow_forwardInhibitors are common in biological systems. Why might some organisms release enzyme inhibitors into their surrounding environment?arrow_forwardWhich of the below is likely a substrate of a kinase? A)insulin B)serine C)phosphate D)ADP E)ATP F)pyruvatearrow_forward
- In noncompetitive inhibition, can both the substrate and the inhibitor bind at the same time? I know the inhibitor changes the enzyme's conformation so it would lower the product formation, but what if the substrate were to bind first, and then the inhibitor binded afterwards?arrow_forwardIt is important for a protease to distinguish between two different proteins so that it only cleaves its target protein. The target protein has the target sequence glu-asp- ser. What amino acids should line the substrate-binding site (the target protein binding site) of the enzyme to help it to recognize its target? Amino acids such as glutamate and aspartate. Amino acids such as glutamine and phenylalanine. Amino acids such as arginine and lysine. Amino acids such as tryptophan and cysteine. Any amino acids would work as long as there are three.arrow_forwarda) b) You walk into university and see that everyone has become a unicorn. You try to hide in bluezone only to figure out that everyone can sense you. You are kidnapped by a unicorn, and they ask you: "How do kinases work?" You wake up realizing it was all a dream, but you still wonder: how do kinases work? Hydrolyze the protein and then ATP to activate it First hydrolyze ATP and then transfer Pi to activate a protein Tranfer a free Pi and then hydrolyze ATP to make more free Pi Bind GTP after releasing GDP from the alpha subunitarrow_forward
- You think you need may have found a new inhibitor (NI) of the HIV protease, so you performed few experiments to characterize its behavior. You found that if you add an excess of substrate to the protease in the presence of the inhibitor, enzyme activity decreased at low substrate but reached the same vmax as observed in the absence of the inhibitor. Also, the affinity of the substrate for the enzyme is decreased by the inhibitor. What class of inhibitor is NI, competitive, uncompetitive, non competitive, or mixed type?arrow_forwardThe video showed one way that a G protein-coupled receptor (GPCR) can deliver a signal using heterotrimeric G proteins. Place the steps in this signal transduction pathway in the correct order, starting with the earliest on the left and the latest on the right. Drag all steps into the box below, placing them in the correct order from first to last. Avoid stacking answers on top of each other. The Gs alpha subunit dissociates ATP is converted to cyclic AMP First step GDP is exchanged for GTP on the G protein Ligand binding to the GPCR Reset Help Adenylyl cyclase is activated Last steparrow_forwardWhich of the following directly phosphorylate tyrosines to start a kinase protein enzymatic cascade? a) Receptor threonine kinase b) Receptor serine kinase c) Receptor tyrosine kinase d) Receptor guanylyl cyclasesarrow_forward
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